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6jzq

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Current revision (10:40, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6jzq' size='340' side='right'caption='[[6jzq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='6jzq' size='340' side='right'caption='[[6jzq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jzq]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JZQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jzq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JZQ FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Synpcc7942_1594, SEC0028 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.798&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Long-chain_acyl-[acyl-carrier-protein]_reductase Long-chain acyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.80 1.2.1.80] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzq OCA], [https://pdbe.org/6jzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jzq RCSB], [https://www.ebi.ac.uk/pdbsum/6jzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzq ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzq OCA], [http://pdbe.org/6jzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jzq RCSB], [http://www.ebi.ac.uk/pdbsum/6jzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AAR_SYNE7 AAR_SYNE7]] Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.<ref>PMID:20671186</ref>
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[https://www.uniprot.org/uniprot/AAR_SYNE7 AAR_SYNE7] Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.<ref>PMID:20671186</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Long-chain alk(a/e)nes represent the major constituents of conventional transportation fuels. Biosynthesis of alkanes is ubiquitous in many kinds of organisms. Cyanobacteria possess two enzymes, acyl-acyl carrier protein (acyl-ACP) reductase (AAR) and aldehyde-deformylating oxygenase (ADO), which function in a two-step alkane biosynthesis pathway. These two enzymes act in series and possibly form a complex that efficiently converts long chain fatty acyl-ACP/fatty acyl-CoA into hydrocarbon. While the structure of ADO has been previously described, structures of both AAR and AAR-ADO complex have not been solved, preventing deeper understanding of this pathway. Here, we report a ligand-free AAR structure, and three AAR-ADO complex structures in which AARs bind various ligands. Our results reveal the binding pattern of AAR with its substrate/cofactor, and suggest a potential aldehyde-transferring channel from AAR to ADO. Based on our structural and biochemical data, we proposed a model for the complete catalytic cycle of AAR.
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Structural insights into catalytic mechanism and product delivery of cyanobacterial acyl-acyl carrier protein reductase.,Gao Y, Zhang H, Fan M, Jia C, Shi L, Pan X, Cao P, Zhao X, Chang W, Li M Nat Commun. 2020 Mar 23;11(1):1525. doi: 10.1038/s41467-020-15268-y. PMID:32251275<ref>PMID:32251275</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6jzq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anacystis nidulans r2]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, Y]]
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[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
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[[Category: Li, M]]
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[[Category: Gao Y]]
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[[Category: Zhang, H M]]
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[[Category: Li M]]
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[[Category: Aldehyde]]
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[[Category: Zhang HM]]
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[[Category: Alkane]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Reductase]]
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Current revision

The crystal structure of acyl-acyl carrier protein (acyl-ACP) reductase (AAR)

PDB ID 6jzq

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